Literature DB >> 241417

Sialic acid, electrophoretic mobility and transmembrane potentials of the Amphiuma red cell.

L Pape, B I Kristensen, O Bengtson.   

Abstract

Red cells from the giant salamander Amphiuma means are shown to contain sialic acid. The amount removed by the action of neuraminidase is equal to that released by acid hydrolysis, indicating that all of the sialic acid is present on the outer surface of the plasma membrane. These cells have a negative electrophoretic mobility and 100% enzymatic removal of sialic acid results in a 40% reduction in the mobility, suggesting that either a fraction of the sialic acid carboxyl groups are unavailable to the action of external electric fields, or other negatively charged groups contribute to the surface charge. A further reduction in mobility of normal and sialic acid-free cells is caused by an increased extracellular calcium concentration. The negative groups affected by calcium are most likely to be phosphate groups, since the isoelectric point of the cells is found to lie between the pK values for H2PO-4 groups and the carboxyl groups of sialic acid. Membrane potentials of single cells, from which 80% or more of the total sialic acid had been removed, were identical to those measured in normal cells, confirming that sialic acid plays little, if any, direct role in the maintenance of membrane potentials and ionic permeabilities.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 241417     DOI: 10.1016/0005-2736(75)90029-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Effects of exogenous neuraminidase on unit activity in frog spinal cord and fish optic tectum.

Authors:  H Römer; H Rahmann
Journal:  Exp Brain Res       Date:  1979-01-02       Impact factor: 1.972

2.  Enforced adhesion of hematopoietic cells to culture dish induces endomitosis and polyploidy.

Authors:  Xuan Huang; Wei Dai; Zbigniew Darzynkiewicz
Journal:  Cell Cycle       Date:  2005-06-15       Impact factor: 4.534

3.  Phylogenetic Distribution of CMP-Neu5Ac Hydroxylase (CMAH), the Enzyme Synthetizing the Proinflammatory Human Xenoantigen Neu5Gc.

Authors:  Sateesh Peri; Asmita Kulkarni; Felix Feyertag; Patricia M Berninsone; David Alvarez-Ponce
Journal:  Genome Biol Evol       Date:  2018-01-01       Impact factor: 3.416

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.